2023
Arabidopsis Tubby domain‐containing F‐box proteins positively regulate immunity by modulating PI4Kβ protein levels
Devendrakumar K, Copeland C, Adamchek C, Zhong X, Huang X, Gendron J, Li X. Arabidopsis Tubby domain‐containing F‐box proteins positively regulate immunity by modulating PI4Kβ protein levels. New Phytologist 2023, 240: 354-371. PMID: 37571862, PMCID: PMC11114105, DOI: 10.1111/nph.19187.Peer-Reviewed Original ResearchConceptsTubby-like proteinsN-terminal F-box domainF-box E3 ligase complexesImmunoprecipitation-mass spectrometry analysisArabidopsis Immune ResponsesPlant immune responsesProtein levelsDomain-containing proteinsF-box domainF-box proteinsE3 ligase complexProteasome-dependent mannerRedundant homologsOverexpression linesTubby domainUbiquitination substratesSkp1-CullinTLP functionsLigase complexTubby proteinBiosynthesis enzymesDouble mutantMass spectrometry analysisProtein 6Novel mechanism
2022
Sugar sensation and mechanosensation in the egg-laying preference shift of Drosophila suzukii
Wang W, Dweck H, Talross G, Zaidi A, Gendron J, Carlson J. Sugar sensation and mechanosensation in the egg-laying preference shift of Drosophila suzukii. ELife 2022, 11: e81703. PMID: 36398882, PMCID: PMC9674340, DOI: 10.7554/elife.81703.Peer-Reviewed Original ResearchConceptsEgg-laying preferenceTaste organsAgricultural pestsDrosophila suzukiiChannel genesStiff substratesDrosophilaTaste sensillaReceptor geneMechanosensory cuesFruit sugarsGenesMechanosensationTaste sensationBitter taste sensationSpeciesEggsSweet taste sensationMajor subsetSuzukiiPestsSugarsElectrophysiological responsesWeak preferenceVariety of changes
2020
Same Concept Different Outcomes: Sugars Determine Circadian Clock Protein Fate in Animals and Plants
Liu W, Gendron J. Same Concept Different Outcomes: Sugars Determine Circadian Clock Protein Fate in Animals and Plants. Molecular Plant 2020, 13: 360-362. PMID: 32092448, DOI: 10.1016/j.molp.2020.02.013.Peer-Reviewed Original Research
2015
The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins
Higgins R, Gendron JM, Rising L, Mak R, Webb K, Kaiser SE, Zuzow N, Riviere P, Yang B, Fenech E, Tang X, Lindsay SA, Christianson JC, Hampton RY, Wasserman SA, Bennett EJ. The Unfolded Protein Response Triggers Site-Specific Regulatory Ubiquitylation of 40S Ribosomal Proteins. Molecular Cell 2015, 59: 35-49. PMID: 26051182, PMCID: PMC4491043, DOI: 10.1016/j.molcel.2015.04.026.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell SurvivalDrosophilaEIF-2 KinaseEndoplasmic ReticulumEndoplasmic Reticulum StressEukaryotic Initiation Factor-2Gene Expression RegulationHumansMolecular Sequence DataPhosphorylationProtein BiosynthesisRibosome Subunits, Small, EukaryoticSaccharomyces cerevisiaeUbiquitinationUnfolded Protein ResponseConceptsUnfolded protein responseRegulatory ubiquitylationRibosomal proteinsUPR activationEukaryotic translational controlUbiquitin-dependent regulationER-resident proteinsChronic UPR activationTranslational reprogrammingER homeostasisTranslational controlCytoplasmic ribosomesProtein foldingTranslation inhibitionProtein responseUbiquitylationPERK signalingUbiquitin proteomicsOptimal cell survivalCell survivalProtein synthesisProteinDegradation capacityReprogrammingActivation